• 제목/요약/키워드: Catalase Activity

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식물체의 catalase 활성에 미치는 아황산가스의 영향 (Effects of Sulfur Dioxide on Catalase Activity in Plants)

  • 성민웅
    • Journal of Plant Biology
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    • 제17권1호
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    • pp.3-8
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    • 1974
  • The experiments were conducted to examine the effects of sulfur dioxide on catalase activity in germinating seeds under dark conditions and in green plants under light conditions. Three kinds of plants, bean (Glycine max M.), cabbage (Brassica oleracea L. Chungbang No.1) and rice (Oryza sativa L. Suwon No.213-1) were used in this study. Both thegerminating seeds and the leaves were treated with various concentrations of sulfur dioxide for both one green plants with two and twelve hours. In the results of the measurement of catalase activity it was found that plant injuries by sulfur dioxide for the period of photosynthesis were higher than those for the period of respiration. In the control, apparent catalase activity under the light condition of photosynthesis showed a considerable decrease in comparison with catalase activity under the dark condition of respiration. This tendency also appeared markedly in the gas treatment. In the gas treatment for twelve hours, the decrease of catalase activity was higher than that of one hour in both photosynthesis and respiraton. It was thought that sulfur dioxide was an inhibitor of catalase activity in higher concentration of the gas.

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Commercial Production and Separation of Catalase Produced by Micrococcus sp.

  • Lee, Ho;Suh, Hyung-Joo;Yu, Hee-Jong;So, Sung;Oh, Sung-Hoon
    • Preventive Nutrition and Food Science
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    • 제7권1호
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    • pp.28-32
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    • 2002
  • A Micrococcus sp. producing catalase was isolated from soil, and a commercial-scathe cultivation and purification of catalase were conducted. The maximum catalase activity was about 103 BU/mL obtained after 46 hr of cultivation in a 30 L fermenter containing 2% glucose, 2% peptone, 4% yeast extract, and 0.5% NaCl. Soybean sauce, CSL (corn steep liquor), and yeast extract were also studied as media substitutes in the media 30 L fermenter. The optimum medium components for the production catalase were found to be 2% glucose, 4% soybean sauce, and 16% CSL. In a 18 kL fermenter, the stationary phase in the cell growth and maximum catalase activity (112 BU/mL) were reached after 46 hr of cultivation, which was the same result as in the 30 L fermenter. The catalase activity was purified with over 17 folds in four steps with a 33.6% yield. From 104,250 mg of protein after cell lysis, 1,966 mg of the purified enzyme with a specific activity of 192.7 kBU/mg was obtained. The residual activity with the addition of 10% NaCl exhibited more than 100%. The use of just NaCl produced a higher residual activity than combination of bencol (benzyldimethyl ammoniumchloride) and PG (propyleneglycol).

홍삼 투여가 방사선에 조사된 생쥐 신장의 Superoxide Dismutase에 미치는 영향 (The Effect of Red Ginseng Extract on Superoxide Dismutase Activity in the Kidney of Gamma-ray Irradiated Mice)

  • 박영순
    • 대한방사선기술학회지:방사선기술과학
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    • 제15권1호
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    • pp.123-130
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    • 1992
  • 감마선에 조사된 흰쥐의 신장 내의 효소활성에 홍삼 추출물이 어떠한 영향을 미치는지를 연구하고자 생후 5주령의 생쥐를 4군으로 분류하여 감마선 조사 및 홍삼 추출물 투여 혹은 생리적 식염수를 투여하고 그로부터 1일, 2일, 3일, 4일 및 5일 등 5회에 걸쳐 도살하여 신장을 취하고 신장조직 내의 SOD, peroxidase 및 catalase 등의 활성도를 측정하였다. 그 결과 홍삼 추출물 투여군은 대조군에 비하여 SOD나 catalase 및 peroxidase의 활성이 유의성있게 증가하다가 회복하였으며 감마선 조사 후 생리적 식염수 투여군은 대조군에 비하여 SOD, peroxidase 및 catalase의 활성이 증가하다가 감소하는 경향이었다. 감마선 조사후 홍삼 추출물 투여군은 SOD, peroxidase 및 catalase의 활성도가 감마선 조사 후 생리적 식염수 투여군에 비하여 보다 빠르게 회복되는 경향이었다. 그러므로 홍삼 추출물이 이온화 방사선 조사 후 장해로 일어나는 SOD, peroxidase 및 catalase 활성도의 변화에 회복효과가 있음이 나타났다.

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Purification and Characterization of a Catalase from Photosynthetic Bacterium Rhodospirillum rubrum S1 Grown under Anaerobic Conditions

  • Kang Yoon-Suk;Lee Dong-Heon;Yoon Byoung-Jun;Oh Duck-Chul
    • Journal of Microbiology
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    • 제44권2호
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    • pp.185-191
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    • 2006
  • The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH $(5.0{\sim}9.0)$, and remained stable over a broad temperature range $(20^{\circ}C{\sim}60^{\circ}C)$. It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19 % of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50 % at concentrations of $11.5{\mu}M,\;0.52{\mu}M,\;and\;0.11{\mu}M$, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase.

Iso-catalase Profiles of Deinococcus spp.

  • Soung, Nak-Kuyn;Lee, Young-Nam
    • BMB Reports
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    • 제33권5호
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    • pp.412-416
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    • 2000
  • The obligate aerobic Deinococcus are highly resistant against lethal effect of UV-and ionizing-radiation. Only five mesophilic Deinococcus species, i. e. D. radiodurans, D. radiophilus, D. proteolyticus, D. radiopugnans, and D. grandis are known. Since an indispensable role of catalase has been suggested in protecting cells against oxidative stress and UV radiation, Deinococcal catalase activity of each species and electrophoretic profiles of catalases were investigated on gel. Total catalase activity was varied among the species in the aerobically grown culture at stationary phase. The occurrence of multiple forms of catalases with different molecular weights in four species of Deinococcus and of a single catalase in D. radiopugnans suggests that each species shows the unique catalase profiles on gel. Some Deinococcal catalases also exhibit peroxidase activity. Since Deinococcus spp. are less-distinct to each other in their morphology, biochemical and physiological properties, the catalase profiles on PAGE would be useful in identifying the species of Deinococcus.

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Differential Expression of Three Catalase Genes in Hot Pepper (Capsicum annuum L.)

  • Lee, Sang Ho;An, Chung Sun
    • Molecules and Cells
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    • 제20권2호
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    • pp.247-255
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    • 2005
  • Three different catalase cDNA clones (CaCat1, CaCat2, and CaCat3) were isolated from hot pepper (Capsicum annuum L.), and their expression patterns were analyzed at the levels of mRNA and enzyme activity. Northern hybridization showed that the three catalase genes were differentially expressed in various organs, and that expression of CaCat1 and CaCat2 was regulated differently by the circadian rhythm. In situ hybridization revealed different spatial distributions of CaCat1 and CaCat2 transcripts in leaf and stem. In response to wounding and paraquat treatment, CaCat1 mRNA increased at 4-12 h in both paraquat-treated and systemic leaves. In contrast, wounding had no significant effect on expression of the catalase genes. The increase of catalase activity in the paraquat-treated and systemic leaves paralleled that of CaCat1 mRNA, but did not match that of CaCat1 mRNA in paraquat-treated stems. Our results suggest that CaCat1 may play a role in responses to environmental stresses.

Growth of Escherichia coli in Iron-enriched Medium Increases HPI Catalase Activity

  • Zaid, Tarrik;Srikumar, Trivandrum Sukumaran Nair;Benov, Ludmil
    • BMB Reports
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    • 제36권6호
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    • pp.608-610
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    • 2003
  • Escherichia coli has two catalases, HPI and HPII. HPI is induced during logarithmic growth in response to low concentrations of hydrogen peroxide. This induction is OxyR-dependent. On the other hand, HPII is not peroxide-inducible but is induced in entry to the stationary phase. We demonstrate here that E. coli displayed higher HPI catalase activity when compared to the cultures that were grown in a normal medium, if grown in a medium supplemented with iron-citrate. Iron supplementation had no effect on HPII catalase. This increase of HPI activity was OxyR-independent and not observed in a ${\Delta}fur$ mutant. The physiological significance of the increase of HPI activity is unclear, but it appears that the katG gene that codes for HPI catalase is among the genes that are regulated by Fur.

치주질환 환자의 말초혈액내 glutathione peroxidase와 catalase의 활성 변화에 관한 연구 (STUDY ON THE ALTERATION OF GLUTATHIONE PEROXIDASE & CATALASE ACTIVITY IN PERIPHERAL BLOOD OF PERIODONTAL DISEASE PATIENTS)

  • 김병옥;김찬진;한경윤
    • Journal of Periodontal and Implant Science
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    • 제25권3호
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    • pp.529-538
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    • 1995
  • It has been believed that the increased release of free oxygen radicals ($O_2^-,H_2O_2$, and $OH^-$) might be a factor in the pathogenesis of periodontal diseases. Antioxidant enzymes such as glutathione peroxidase(GSH-PX) and catalase can protect the tissue damage from the $H_2O_2$. In order to investigate the GSH-PX and catalase activity in the blood plasma and red blood cells(RBCs) of the patients with periodontitis, 19 patients who had good general health, attachment loss more than 6 mm and bone loss were selected as periodontitis group, 7 patients who had severely inflamed gingiva were selected as gingivitis group, and 15 volunteers with good general and periodontal health were selected as normal group. 17 of 26 patients were performed scaling and root planing to reduce the gingival inflammation for gingivitis and periodontitis groups, and were selected as posttreatment group. After blood plasma and RBCs were collected and separated 1 ml of peripheral blood from each subject, GSH-PX activity in blood plasma and RBCs was measured by the same method that Stefan et al. did, and catalase activity in RBCs was measured by the same method that Beers et al. did. The difference of GSH-PX and catalase activity between normal, gingivitis, and periodontitis groups was statistically analyzed by ANOVA with SPSS/PC+ program, and the difference between pretreatment and posttreatment groups was analyzed by Student t-test. The results were as follows : 1. GSH-PX activity in blood plasma was significantly lower in the gingivitis group($0.8683{\pm}0.0658$), periodontitis group($0.7130{\pm}0.1333$) than in the normal group($1.0241{\pm}0.0801$)(p<0.05), and GSH-PX activity in RBCs was significantly lower in the gingivitis groupt. $0.8156{\pm}0.1167$), periodontitis group($0.7533{\pm}0.1185$) than in the normal group($l.1963{\pm}0.2044$)(P<0.05), but there was no statistical significance in the difference of GSH-PX activity in RBCs between the gingivitis group and periodontitis group(p>0.05). 2. Catalase activity in RBCs was siginficantly lower in the periodontitis group($117.34{\pm}35.01$) than in the normal group($l52.38{\pm}32.09$)(p<0.05). 3. GSH-PX activity in blood plasma was significantly increased in the posttreatment groupe $1.0376{\pm}0.2820$) compared to the pretreatment group(0.7608 0.1600) (p<0.05), and GSH-PX activity in RBC was significantly increased in the posttreatment group($1.0421{\pm}0.2330$) compared to the pretreatment group($0.7728{\pm}0.1210$)(p<0.05). 4. There was no statistical significance in the difference of catalase activity in RBCs between the pretreatment group($112.04{\pm}43.65$) and posttreatment group($l33.41{\pm}39.16$)(p>0.05).The results, within the limits of the present experiment, suggest that the lowered activity of GSH-PX and catalase in blood plasma and RBCs may be related with periodontopathogenesis.

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빛과 카드뮴이 벼 catalase 활성과 동위효소 발현에 미치는 영향 (Effect of Light and Cadmium on the Activity and Isozyme Pattern of Catalase from Ric(Oryza sativa L.))

  • 김윤경;이미영
    • Applied Biological Chemistry
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    • 제49권4호
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    • pp.287-292
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    • 2006
  • 명조건과 암조건에서 카드뮴이 벼 유묘 뿌리와 줄기의 카탈라제 총 활성과 동위효소 발현에 미치는 영향을 조사하였다. 카드뮴을 처리하면 명조건과 암조건의 뿌리와 줄기에서 과산화수소 함량이 현저하게 증가하였다. 뿌리의 카탈라제 동위효소는 잎과는 서로 다른 조직 특이적 발현양상을 보여주었다. 또한 카드뮴을 처리하게 되면 명조건 뿌리는 암조건 뿌리와 카탈라제 동위효소의 발현 패턴에 차이를 보였다. 1 mM 카드뮴 처리에 의하여 명조건 뿌리의 카탈라제 총 활성은 약 16배 증가하였는데 이러한 활성증가는 동위효소 CAT1l과 CAT2의 증가에 의한 것이었다. 반면 암조건 뿌리의 카탈라제는 0.1mM 카드뮴에 의하여 약 3배 증가하였느나, 0.5와 1mM카드뮴에 의하여 오히려 효소활성이 감소하였다. 0.1mM카드뮴에 의한 효소활성 증가는 CAT1, CAT3, CAT4 동위효소의 활성 증가에 기인하였으나 카드뮴 농도를 더 높였을때 CAT2와 CAT4가 감소하였다. 대조군 잎에는 양극 동위효소인 CATc, 중성 동위효소인 CATn와 음극 동위효소인 CAT1가 존재하였다. 잎에서는 명조건과 암조건 모두에서 카드뮴을 처리하여도 카탈라제 활성과 동위효소 발현에 차이가 없었다. 이러한 결과들은 카드뮴에 의한 뿌리 카탈라제 효소의 발현변화는 빛에 의하여 조절되지만 잎 카탈라제의 발현은 빛에 의하여 조절되지 않음을 보여준다.

흰쥐에서 Aminotriazole과 Diethyldithiocarbamate가 Paraquat의 독성에 미치는 영향 (Effects of 3-Amino-1,2,4 Triazole and Diethyldithiocarbamate on Paraquat Toxicity in Rats)

  • 차종희;고광삼
    • Toxicological Research
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    • 제13권4호
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    • pp.393-400
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    • 1997
  • The effects of superoxide dismutase(SOD) and catalase on the toxicity of paraquat(PQ) were studied using diethyldithiocarbamate(DDC), 3-amino-1,2,4-triazole(AT) which are inhibitors of Cu, Zn-SOD and catalase in rats. Sprague Dawley rats were divide into 6 groups: control, DDC, PQ, AT, DDC+PQ, and AT+PQ group. The PQ (50 mg/kg body weight(BW); about half dose of $LD_{50}$) was administered with orally, otherwise AT(1.0g/kg BW) and DDC(1.0g/kg BW) were administered by intrperitoneal(iP) injection. The survival rate of rats in PQ+AT group was significantly decreased compared with PQ group while the difference of survival rate between DDC group and DDC+PQ group was not significant. The SOD activity after administration of DDC was decreased in liver, lung and kidney, but catalase activity was not changed. The catalase activity in liver, lung and kidney of AT treated rats was decreased, while SOD activity was not changed in this group. The effects of DDC and AT to the PQ toxicity was also observed in primary cultured rat Skin fibroblasts. The viable cells that was measured with MTT method, was decreased in AT+PQ treated group compared to PQ treated group, but the difference of cell viability between DDC treat group and DDC+PQ treated group was not observed. This result, AT potentlate PQ toxicity while DDC were not affect, suggested that the decreased catalase activity lead to elevation of hydrogen peroxide levels and PQ toxicity may be correlate with the hydrogen peroxide rather than the superoxides.

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